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Neurocognitive derivation of protein surface property from protein aggregate parameters

Current work targeted to predicate parametric relationship between aggregate and individual property of a protein. In this approach, we considered individual property of a protein as its Surface Roughness Index (SRI) which was shown to have potential to classify SCOP protein families. The bulk prope...

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Detalles Bibliográficos
Autores principales: Mishra, Hrishikesh, Lahiri, Tapobrata
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092950/
https://www.ncbi.nlm.nih.gov/pubmed/21572883
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author Mishra, Hrishikesh
Lahiri, Tapobrata
author_facet Mishra, Hrishikesh
Lahiri, Tapobrata
author_sort Mishra, Hrishikesh
collection PubMed
description Current work targeted to predicate parametric relationship between aggregate and individual property of a protein. In this approach, we considered individual property of a protein as its Surface Roughness Index (SRI) which was shown to have potential to classify SCOP protein families. The bulk property was however considered as Intensity Level based Multi-fractal Dimension (ILMFD) of ordinary microscopic images of heat denatured protein aggregates which was known to have potential to serve as protein marker. The protocol used multiple ILMFD inputs obtained for a protein to produce a set of mapped outputs as possible SRI candidates. The outputs were further clustered and largest cluster centre after normalization was found to be a close approximation of expected SRI that was calculated from known PDB structure. The outcome showed that faster derivation of individual protein’s surface property might be possible using its bulk form, heat denatured aggregates.
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spelling pubmed-30929502011-05-13 Neurocognitive derivation of protein surface property from protein aggregate parameters Mishra, Hrishikesh Lahiri, Tapobrata Bioinformation Hypothesis Current work targeted to predicate parametric relationship between aggregate and individual property of a protein. In this approach, we considered individual property of a protein as its Surface Roughness Index (SRI) which was shown to have potential to classify SCOP protein families. The bulk property was however considered as Intensity Level based Multi-fractal Dimension (ILMFD) of ordinary microscopic images of heat denatured protein aggregates which was known to have potential to serve as protein marker. The protocol used multiple ILMFD inputs obtained for a protein to produce a set of mapped outputs as possible SRI candidates. The outputs were further clustered and largest cluster centre after normalization was found to be a close approximation of expected SRI that was calculated from known PDB structure. The outcome showed that faster derivation of individual protein’s surface property might be possible using its bulk form, heat denatured aggregates. Biomedical Informatics 2011-05-07 /pmc/articles/PMC3092950/ /pubmed/21572883 Text en © 2011 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Mishra, Hrishikesh
Lahiri, Tapobrata
Neurocognitive derivation of protein surface property from protein aggregate parameters
title Neurocognitive derivation of protein surface property from protein aggregate parameters
title_full Neurocognitive derivation of protein surface property from protein aggregate parameters
title_fullStr Neurocognitive derivation of protein surface property from protein aggregate parameters
title_full_unstemmed Neurocognitive derivation of protein surface property from protein aggregate parameters
title_short Neurocognitive derivation of protein surface property from protein aggregate parameters
title_sort neurocognitive derivation of protein surface property from protein aggregate parameters
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3092950/
https://www.ncbi.nlm.nih.gov/pubmed/21572883
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